Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 82, Issue 6, Pages 1093-1098Publisher
WILEY
DOI: 10.1002/prot.24481
Keywords
bld mutant; DNA binding; NMR; solution structure; winged helix-turn-helix
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Funding
- Ministry for Health, Welfare & Family Affairs, Republic of Korea [A092006]
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BldD regulates transcription of key developmental genes in Streptomyces coelicolor. While the N-terminal domain is responsible for both dimerization and DNA binding, the structural and functional roles of the C-terminal domain (CTD) remain largely unexplored. Here, the solution structure of the BldD-CTD shows a novel winged-helix domain fold not compatible with DNA binding, due to the negatively charged surface and presence of an additional helix. Meanwhile, a small elongated groove with conserved hydrophobic patches surrounded by charged residues suggests that the BldD-CTD could be involved in protein-protein interactions that provide transcriptional regulation. Proteins 2014; 82:1093-1098. (c) 2013 Wiley Periodicals, Inc.
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